Codon optimization reveals critical factors for high level expression of two rare codon genes in Escherichia coli: RNA stability and secondary structure but not tRNA abundance.

Journal article

Expression patterns in Escherichia coli of two small archaeal proteins with a natural content of about 30% rare codons were analyzed. The proteins, a histone-like protein from Sulfolobus shibatae (Ssh10), and a glutaredoxin-like protein from Methanobacterium thermoautotrophicum (mtGrx), were produced with expression plasmids encoding wild-type genes, codon-optimized synthetic, and GST-fusion genes. These constructs were expressed in BL21 (DE3), its LysS derivative, and modified strains carryi...

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Authors: Wu, X; Jörnvall, H; Berndt, K; Oppermann, U

• Publication status: Published
• Journal: Biochemical and biophysical research communications
• Volume: 313
• Issue: 1
• Pages: 89-96
• Publication date: 2004-01-01
• DOI: 10.1016/j.bbrc.2003.11.091
• EISSN: 1090-2104
• ISSN: 0006-291X
• Language: English
• Keywords: Escherichia coli; Sulfolobus; Spectrometry, Mass, Electrospray Ionization; Protein Structure, Secondary; Protein Biosynthesis; Methanobacterium; RNA, Messenger; Circular Dichroism; RNA, Transfer; Recombinant Fusion Proteins; Codon; Genes, Archaeal; Artificial Gene Fusion; RNA Stability; Archaeal Proteins; Gene Expression Regulation, Bacterial